Crystalline Inclusion

2020 ◽  
Author(s):  
RSC Advances ◽  
2021 ◽  
Vol 11 (22) ◽  
pp. 13091-13096
Author(s):  
Lu Chen ◽  
Yanbin Huang

Guest polymers have significant influence on the dissolution of drug–polymer inclusion complex crystals.


2014 ◽  
Vol 35 (4) ◽  
pp. 627-646 ◽  
Author(s):  
Irena Giełwanowska ◽  
Marta Pastorczyk ◽  
Maja Lisowska ◽  
Michał Węgrzyn ◽  
Ryszard J. Górecki

AbstractThis study investigated leaf mesophyll cells of Caryophyllaceae plants growing in polar regions – Cerastium alpinum and Silene involucrata from the Hornsund region of Spitsbergen island (Svalbard Archipelago, Arctic), and Colobanthus quitensis from the Admiralty Bay region on King George Island (South Shetland Islands, West Antarctic). Ultrastructural changes were analyzed in mesophyll protoplasts of plants growing in natural Arctic and Antarctic habitats and plants grown in a greenhouse, including plants exposed to short-term cold stress under semi-controlled conditions. Cell organelles of plants growing in natural polar habitats and greenhouse-grown plants were characterized by significant morphological plasticity. Chloroplasts of plants studied in this work formed variously shaped protrusions and invaginations that visibly increased the contact area between adjacent cell compartments and reduced the distance between organelles. S. involucrata plants grown under greenhouse conditions, tested by us in this work, were characterized by highly dynamic cell nuclei with single or multiple invaginations of the nuclear membrane and the presence of channels and cisternae filled with cytoplasm and organelles. Crystalline inclusion proteins were observed in the cell nuclei of C. quitensis between nuclear membranes and in the direct proximity of heterochromatin. Our study revealed significant conformational dynamics of organelles, manifested by variations in the optical density of matrices, membranes and envelopes, in particular in C. quitensis, which could suggest that the analyzed Caryophyllaceae taxa are well adapted to severe climate and changing conditions in polar regions.


1979 ◽  
Vol 38 (1) ◽  
pp. 11-22
Author(s):  
K. Esau ◽  
A.C. Magyarosy

The compounds crystalloids formed in sieve element nuclei of Amsinckia douglasiana A. DC. (Boraginaceae) during differentiation of the cell become disaggregated during the nuclear breakdown characteristic of a maturing sieve element. The phenomenon occurs in both healthy and virus-infected plants. The crystalloid component termed cy, which is loosely aggregated, separates from the densely aggregated component termed cx and disperses. The cx component may become fragmented, or broken into large pieces, or remain intact after the cell matures. After their release from the nucleus both crystalloid components become spatially associated with the dispersed P-protein originating in the cytoplasm, but remain distinguishable from it. The component tubules of P-protein are hexagonal in transections and are somewhat wider than the 6-sided cy tubules. The cx tubules are much narrower than the P-protein or the cy tubules and have square transections. Both the P-protein and the products of disintegrated crystalloids accumulate at sieve plates in sieve elements subjected to sudden release of hydrostatic pressure by cutting the phloem. The question of categorizing the tubular components of the nuclear crystalloid of a sieve element with reference to the concept of P-protein is discussed.


2002 ◽  
Vol 35 (9) ◽  
pp. 3778-3780 ◽  
Author(s):  
Xintao Shuai ◽  
Francis E. Porbeni ◽  
Min Wei ◽  
Todd Bullions ◽  
Alan E. Tonelli

2001 ◽  
Vol 67 (10) ◽  
pp. 4834-4841 ◽  
Author(s):  
David J. Bowen ◽  
Jerald C. Ensign

ABSTRACT Cells of the entomopathogenic bacterium Photorhabdus luminescens contain two types of morphologically distinct crystalline inclusion proteins. The larger rectangular inclusion (type 1) and a smaller bipyramid-shaped inclusion (type 2) were purified from cell lysates by differential centrifugation and isopycnic density gradient centrifugation. Both structures are composed of protein and are readily soluble at pH 11 and 4 in 1% sodium dodecyl sulfate (SDS) and in 8 M urea. Electrophoretic analysis reveals that each inclusion is composed of a single protein subunit with a molecular mass of 11,000 Da. The proteins differ in amino acid composition, protease digestion pattern, and immunological cross-reactivity. The protein inclusions are first visible in the cells at the time of late exponential growth. Western blot analyses showed that the proteins appeared in cells during mid- to late exponential growth. When at maximum size in stationary-phase cells, the proteins constitute 40% of the total cellular protein. The protein inclusions are not used during long-term starvation of the cells and were not toxic when injected into or fed toGalleria mellonella larvae.


2007 ◽  
Vol 48 (3) ◽  
pp. 540-546 ◽  
Author(s):  
O. V. Andreeva ◽  
B. F. Garifullin ◽  
A. T. Gubaidullin ◽  
V. A. Al’fonsov ◽  
V. E. Kataev ◽  
...  

2006 ◽  
Vol 930 ◽  
Author(s):  
Robert W. Bradshaw ◽  
Blake A. Simmons ◽  
Eric H Majzoub ◽  
W. Miles Clift ◽  
Daniel E. Dedrick

ABSTRACTClathrate hydrates are crystalline inclusion compounds of water and a guest molecule (e.g., methane) that form at temperatures below ambient but above the freezing point of water. There are three known crystalline structures of hydrates (structure I, II, and H) in which cavities within the hydrogen bonded water molecule lattice trap the hydrate-forming species. The clathrate structure excludes dissolved solutes, such as sodium chloride, from the aqueous phase and thereby offers a possible means to produce potable water from seawater or brackish water. The concept of using clathrate hydrates for desalination is not new. However, before clathrate hydrate desalination becomes a viable technology, fundamental issues of controlled hydrate formation, hydrate size and morphology, agglomeration, amount of entrapped salt, and the efficient recovery of hydrates must be understood. This paper will report structural characterization of hydrates formed with several guest molecules over a wide range of conditions in an attempt to further the physicochemical insight needed to address these issues.Clathrate hydrate formation experiments were performed using a variety of host molecules, including R141b, a commercial refrigerant, C2FCl2H3. Hydrates of R141b were formed at temperatures from 2°C to 6°C and atmospheric pressure from deionized water and 2% - 7% NaCl solutions. Samples of the hydrates were characterized by cold-stage x-ray diffraction and Raman spectroscopy and determined to be structure II. Additional experiments were conducted with a gaseous hydrate former, ethylene, which readily formed hydrates with deionized or saline water at 2°C and several atmospheres of pressure. Experiments with several other hydrate forming molecules were conducted and the results obtained from their structural characterization will be reported. We will also present proof-of-concept experiments demonstrating a novel technique of desalination using these hydrate formers.Sandia National Laboratories is a multiprogram laboratory operated by Sandia Corporation, a Lockheed Martin company, for the United States Department of Energy under contract DE-AC04-94AL85000.


1990 ◽  
Vol 110 (3) ◽  
pp. 669-679 ◽  
Author(s):  
L Bomblies ◽  
E Biegelmann ◽  
V Döring ◽  
G Gerisch ◽  
H Krafft-Czepa ◽  
...  

Developing cells of Dictyostelium discoideum contain crystalline inclusion bodies. The interlattice spaces of the crystals are approximately 11 nm, and their edge dimensions vary in aggregating cells from 0.1 to 0.5 micron. The crystals are enclosed by a membrane with the characteristics of RER. To unravel the nature of the crystals we isolated them under electron microscopical control and purified the two major proteins that cofractionate with the crystals, one of an apparent molecular mass of 69 kD, the other of 56 kD. This latter protein proved to be identical with the protein encoded by the developmentally regulated D2 gene of D. discoideum, as shown by its reactivity with antibodies raised against the bacterially expressed product of a D2 fusion gene. The D2 gene is known to be strictly regulated at the transcript level and to be controlled by cAMP signals. Accordingly, very little of the 56-kD protein was detected in growth phase cells, maximal expression was observed at the aggregation stage, and the expression was stimulated by cAMP pulses. The 69-kD protein is the major constituent of the crystals and is therefore called "crystal protein." This protein is developmentally regulated and accumulates in aggregating cells similar to the D2 protein, but is not, or is only slightly regulated by cAMP pulses. mAbs specific for either the crystal protein or the D2 protein, labeled the intracellular crystals as demonstrated by the use of immunoelectron microscopy. The complete cDNA-derived amino acid sequence of the crystal protein indicates a hydrophobic leader and shows a high degree of sequence similarity with Torpedo acetylcholinesterase and rat lysophospholipase. Because the D2 protein also shows sequence similarities with various esterases, the vesicles filled with crystals of these proteins are named esterosomes.


Sign in / Sign up

Export Citation Format

Share Document